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    RAB1B RAB1B, member RAS oncogene family [ Homo sapiens (human) ]

    Gene ID: 81876, updated on 3-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    MicroR-380-3p Reduces Sepsis-Induced Acute Kidney Injury via Regulating RAB1P to Restrain NF-kappaB Pathway.

    MicroR-380-3p Reduces Sepsis-Induced Acute Kidney Injury via Regulating RAB1P to Restrain NF-κB Pathway.
    Liang J, Li B, Xia Y.

    10/1/2024
    Circ_RBM23 knockdown suppresses chemoresistance, proliferation, migration and invasion of sorafenib-resistant HCC cells through miR-338-3p/RAB1B axis.

    Circ_RBM23 knockdown suppresses chemoresistance, proliferation, migration and invasion of sorafenib-resistant HCC cells through miR-338-3p/RAB1B axis.
    Xu C, Sun W, Liu J, Pu H, Li Y.

    05/20/2023
    Dephosphocholination by Legionella effector Lem3 functions through remodelling of the switch II region of Rab1b.

    Dephosphocholination by Legionella effector Lem3 functions through remodelling of the switch II region of Rab1b.
    Kaspers MS, Pogenberg V, Pett C, Ernst S, Ecker F, Ochtrop P, Groll M, Hedberg C, Itzen A., Free PMC Article

    04/24/2023
    LINC00173 facilitates tumor progression by stimulating RAB1B-mediated PA2G4 and SDF4 secretion in nasopharyngeal carcinoma.

    LINC00173 facilitates tumor progression by stimulating RAB1B-mediated PA2G4 and SDF4 secretion in nasopharyngeal carcinoma.
    He SW, Liang YL, Zhang Y, Liu X, Gong S, Ye ML, Huang SY, Tan XR, Zhou SQ, Zhao Y, Liu N, Li YQ., Free PMC Article

    03/9/2023
    Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1.

    Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1.
    Du J, Wrisberg MV, Gulen B, Stahl M, Pett C, Hedberg C, Lang K, Schneider S, Itzen A., Free PMC Article

    02/6/2021
    RAB1b interacts with TRAF3 to promote antiviral innate immunity.

    The small GTPase RAB1B promotes antiviral innate immunity by interacting with TNF receptor-associated factor 3 (TRAF3).
    Beachboard DC, Park M, Vijayan M, Snider DL, Fernando DJ, Williams GD, Stanley S, McFadden MJ, Horner SM., Free PMC Article

    05/23/2020
    ARF5 and Rab1b exhibit RNA-binding capacity, suggesting a role for domain 3 of the IRES in RNA localization into specific cellular compartments.

    Rab1b and ARF5 are novel RNA-binding proteins involved in FMDV IRES-driven RNA localization.
    Fernandez-Chamorro J, Francisco-Velilla R, Ramajo J, Martinez-Salas E., Free PMC Article

    02/29/2020
    Rab1b differentially controls the secretion of apolipoproteins and of HCV.

    Differential Regulation of Lipoprotein and Hepatitis C Virus Secretion by Rab1b.
    Takacs CN, Andreo U, Dao Thi VL, Wu X, Gleason CE, Itano MS, Spitz-Becker GS, Belote RL, Hedin BR, Scull MA, Rice CM, Simon SM., Free PMC Article

    06/16/2018
    Survival analysis indicates that patients with overexpression of Rab1B or MMP9 have significantly worse overall survival and progression-free survival, but better response to chemotherapy than those with low expression of proteins, and that Rab1B is an independent prognostic factor for colorectal cancer patients.

    Overexpression of Rab1B and MMP9 predicts poor survival and good response to chemotherapy in patients with colorectal cancer.
    Yang XZ, Cui SZ, Zeng LS, Cheng TT, Li XX, Chi J, Wang R, Zheng XF, Wang HY., Free PMC Article

    11/18/2017
    In these Rab1B-depleted cells, ATG9A accumulated in intermediate membrane structures at autophagosome formation sites. These results indicate that Rab1B is involved in regulating the proper development of autophagosomes.

    Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation.
    Kakuta S, Yamaguchi J, Suzuki C, Sasaki M, Kazuno S, Uchiyama Y.

    10/14/2017
    Authors demonstrate that Rap1b expression is aberrantly increased in GC, resulting in the inhibition of autophagy and apoptosis of GC cells by the PI3K/Akt/mTOR pathway.

    Knockdown of Rap1b Enhances Apoptosis and Autophagy in Gastric Cancer Cells via the PI3K/Akt/mTOR Pathway.
    Li Y, Liu Y, Shi F, Cheng L, She J., Free PMC Article

    04/8/2017
    RAB1B localization to the Golgi.

    PITPNC1 Recruits RAB1B to the Golgi Network to Drive Malignant Secretion.
    Halberg N, Sengelaub CA, Navrazhina K, Molina H, Uryu K, Tavazoie SF., Free PMC Article

    07/30/2016
    RAB1B acts as a metastasis suppressor in triple-negative breast cancer by regulating the TGF-beta/SMAD signaling pathway and RAB1B may serve as a biomarker of prognosis and response to anti-tumor therapeutics for patients with triple-negative breast cancer.

    Loss of RAB1B promotes triple-negative breast cancer metastasis by activating TGF-β/SMAD signaling.
    Jiang HL, Sun HF, Gao SP, Li LD, Hu X, Wu J, Jin W., Free PMC Article

    04/30/2016
    Our results show, for the first time, that changes in Rab1b levels modulate gene transcription and strongly suggest that a Rab1b increase is required to elicit a secretory response.

    Rab1b overexpression modifies Golgi size and gene expression in HeLa cells and modulates the thyrotrophin response in thyroid cells in culture.
    Romero N, Dumur CI, Martinez H, García IA, Monetta P, Slavin I, Sampieri L, Koritschoner N, Mironov AA, De Matteis MA, Alvarez C., Free PMC Article

    09/14/2013
    The crystal structure of the Rab1b-LepB complex.

    Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB.
    Mihai Gazdag E, Streller A, Haneburger I, Hilbi H, Vetter IR, Goody RS, Itzen A., Free PMC Article

    07/27/2013
    results indicate that the cellular localization of MTMR6 is regulated by Rab1B in the early secretory and autophagic pathways

    Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6) is regulated by small GTPase Rab1B in the early secretory and autophagic pathways.
    Mochizuki Y, Ohashi R, Kawamura T, Iwanari H, Kodama T, Naito M, Hamakubo T., Free PMC Article

    03/30/2013
    The detailed molecular reaction mechanism of a complex between human Rab and RabGAP at the highest possible spatiotemporal resolution and in atomic detail, is described.

    Catalytic mechanism of a mammalian Rab·RabGAP complex in atomic detail.
    Gavriljuk K, Gazdag EM, Itzen A, Kötting C, Goody RS, Gerwert K., Free PMC Article

    02/23/2013
    Rab1a/b and Rab43, are important for herpes simplex virus 1 virion assembly

    Analysis of Rab GTPase-activating proteins indicates that Rab1a/b and Rab43 are important for herpes simplex virus 1 secondary envelopment.
    Zenner HL, Yoshimura S, Barr FA, Crump CM., Free PMC Article

    10/8/2011
    Rab1b is a key regulatory component of COPII dynamics and function.

    Role of Rab1b in COPII dynamics and function.
    Slavin I, García IA, Monetta P, Martinez H, Romero N, Alvarez C.

    06/18/2011
    Antibacterial autophagy occurs at omegasomes and reveal that the Rab1 GTPase plays a crucial role in mammalian autophagy.

    Antibacterial autophagy occurs at PI(3)P-enriched domains of the endoplasmic reticulum and requires Rab1 GTPase.
    Huang J, Birmingham CL, Shahnazari S, Shiu J, Zheng YT, Smith AC, Campellone KG, Heo WD, Gruenheid S, Meyer T, Welch MD, Ktistakis NT, Kim PK, Klionsky DJ, Brumell JH., Free PMC Article

    03/26/2011
    The authors demonstrate that Rab1b-activated GBF1 and ARF1 are involved in Ebolavirus virion formation, suggesting that both the COPII and COPI transport systems play a role in Ebolavirus VP40-mediated particle formation.

    Role of the GTPase Rab1b in ebolavirus particle formation.
    Yamayoshi S, Neumann G, Kawaoka Y., Free PMC Article

    05/3/2010
    findings show that SidM from Legionella pneumophila could act as both a GDP-GTP exchange factor and GDP-dissociation inhibitor-displacement factor (GDF) for Rab1

    A bifunctional bacterial protein links GDI displacement to Rab1 activation.
    Machner MP, Isberg RR.

    01/21/2010
    These data support a model where Rab1b-GTP induces GBF1 recruitment at the ERES interface and at the Golgi complex where it is required for COPII/COPI exchange or COPI vesicle formation, respectively.

    Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association.
    Monetta P, Slavin I, Romero N, Alvarez C., Free PMC Article

    01/21/2010
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